Journal
BIOPHYSICAL CHEMISTRY
Volume 109, Issue 3, Pages 333-344Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bpc.2003.12.005
Keywords
netropsin; ligand; nuclear magnetic resonance (NMR); deoxyribo nucleic acid (DNA); drug; chemical shift; carbon; inhibitor
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The antibiotic drug, netropsin, was complexed with the DNA oligonucleotide duplex [d(GGTATACC)](2) to monitor drug C-13 NMR chemical shifts changes. The binding mode of netropsin to the minor groove of DNA is well-known, and served as a good model for evaluating the relative sensitivity of 13C chemical shifts to hydrogen bonding. Large downfield shifts were observed for four resonances of carbons that neighbor sites which are known to form hydrogen bond interactions with the DNA minor groove. Many of the remaining resonances of netropsin exhibit shielding or relatively smaller deshielding changes. Based on the model system presented here, large deshielding NMR shift changes of a ligand upon macromolecule binding can likely be attributed to hydrogen bond formation at nearby sites. (C) 2003 Elsevier B.V. All rights reserved.
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